Title

Role of Ser216 in the Mechanism of Action of Membrane-bound Lytic Transglycosylase B: Further Evidence for Substrate-assisted Catalysis

Authors

Christopher W. Reid, Bryant University
Blaine A. Legaree
Anthony J. ClarkeFollow

Document Type

Article

Comments

Published by the Federation of European Biochemical Societies in FEBS Letters Volume 581, Issue 25, pages 4988-4992.

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Keywords

Lytic transglycosylase;Substrate-assisted catalysis;Site-directed mutagenesis

Publisher

Federation of European Biochemical Societies

Publication Source

FEBS Letters

Abstract

Lytic transglycosylases cleave the β-(1 → 4)-glycosidic bond in the bacterial cell wall heteropolymer peptidoglycan between the N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues with the concomitant formation of a 1,6-anhydromuramoyl residue. Based on sequence alignments, Ser216 in Pseudomonas aeruginosa membrane-bound lytic transglycosylase B (MltB) was targeted for replacement with alanine to delineate its role in the enzyme’s mechanism of action.